Assembling the Tat protein translocase
The twin-arginine protein translocation system (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membranes of plant chloroplasts. The Tat transporter is assembled from multiple copies of the membrane proteins TatA, TatB, and TatC. We combine sequence co-evo...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications Ltd
2016-12-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/20718 |
| _version_ | 1811200148438515712 |
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| author | Felicity Alcock Phillip J Stansfeld Hajra Basit Johann Habersetzer Matthew AB Baker Tracy Palmer Mark I Wallace Ben C Berks |
| author_facet | Felicity Alcock Phillip J Stansfeld Hajra Basit Johann Habersetzer Matthew AB Baker Tracy Palmer Mark I Wallace Ben C Berks |
| author_sort | Felicity Alcock |
| collection | DOAJ |
| description | The twin-arginine protein translocation system (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membranes of plant chloroplasts. The Tat transporter is assembled from multiple copies of the membrane proteins TatA, TatB, and TatC. We combine sequence co-evolution analysis, molecular simulations, and experimentation to define the interactions between the Tat proteins of Escherichia coli at molecular-level resolution. In the TatBC receptor complex the transmembrane helix of each TatB molecule is sandwiched between two TatC molecules, with one of the inter-subunit interfaces incorporating a functionally important cluster of interacting polar residues. Unexpectedly, we find that TatA also associates with TatC at the polar cluster site. Our data provide a structural model for assembly of the active Tat translocase in which substrate binding triggers replacement of TatB by TatA at the polar cluster site. Our work demonstrates the power of co-evolution analysis to predict protein interfaces in multi-subunit complexes. |
| first_indexed | 2024-04-12T02:00:04Z |
| format | Article |
| id | doaj.art-3bef166b8ab14bf5bf707430b8eb70e3 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T02:00:04Z |
| publishDate | 2016-12-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-3bef166b8ab14bf5bf707430b8eb70e32022-12-22T03:52:42ZengeLife Sciences Publications LtdeLife2050-084X2016-12-01510.7554/eLife.20718Assembling the Tat protein translocaseFelicity Alcock0Phillip J Stansfeld1Hajra Basit2Johann Habersetzer3Matthew AB Baker4Tracy Palmer5Mark I Wallace6https://orcid.org/0000-0002-5692-8313Ben C Berks7https://orcid.org/0000-0001-9685-4067Department of Biochemistry, University of Oxford, Oxford, United KingdomDepartment of Biochemistry, University of Oxford, Oxford, United KingdomDepartment of Chemistry, University of Oxford, Oxford, United KingdomDivision of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, United KingdomDepartment of Chemistry, University of Oxford, Oxford, United KingdomDivision of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, United KingdomDepartment of Chemistry, University of Oxford, Oxford, United KingdomDepartment of Biochemistry, University of Oxford, Oxford, United KingdomThe twin-arginine protein translocation system (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membranes of plant chloroplasts. The Tat transporter is assembled from multiple copies of the membrane proteins TatA, TatB, and TatC. We combine sequence co-evolution analysis, molecular simulations, and experimentation to define the interactions between the Tat proteins of Escherichia coli at molecular-level resolution. In the TatBC receptor complex the transmembrane helix of each TatB molecule is sandwiched between two TatC molecules, with one of the inter-subunit interfaces incorporating a functionally important cluster of interacting polar residues. Unexpectedly, we find that TatA also associates with TatC at the polar cluster site. Our data provide a structural model for assembly of the active Tat translocase in which substrate binding triggers replacement of TatB by TatA at the polar cluster site. Our work demonstrates the power of co-evolution analysis to predict protein interfaces in multi-subunit complexes.https://elifesciences.org/articles/20718Tat protein transportsequence co-evolutionmembrane proteintwin-arginine |
| spellingShingle | Felicity Alcock Phillip J Stansfeld Hajra Basit Johann Habersetzer Matthew AB Baker Tracy Palmer Mark I Wallace Ben C Berks Assembling the Tat protein translocase eLife Tat protein transport sequence co-evolution membrane protein twin-arginine |
| title | Assembling the Tat protein translocase |
| title_full | Assembling the Tat protein translocase |
| title_fullStr | Assembling the Tat protein translocase |
| title_full_unstemmed | Assembling the Tat protein translocase |
| title_short | Assembling the Tat protein translocase |
| title_sort | assembling the tat protein translocase |
| topic | Tat protein transport sequence co-evolution membrane protein twin-arginine |
| url | https://elifesciences.org/articles/20718 |
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